Significance of [2Fe-2S] Cluster N1a for Electron Transfer and Assembly of Escherichia coli Respiratory Complex I

Biochemistry
Katerina DörnerThorsten Friedrich

Abstract

NADH:ubiquinone oxidoreductase, respiratory complex I, couples electron transfer from NADH to ubiquinone with proton translocation across the membrane. NADH reduces a noncovalently bound FMN, and the electrons are transported further to the quinone reduction site by a 95 Å long chain of seven iron-sulfur (Fe-S) clusters. Binuclear Fe-S cluster N1a is not part of this long chain but is located within electron transfer distance on the opposite site of FMN. The relevance of N1a to the mechanism of complex I is not known. To elucidate its role, we individually substituted the cysteine residues coordinating N1a of Escherichia coli complex I by alanine and serine residues. The mutations led to a significant loss of the NADH oxidase activity of the mutant membranes, while the amount of the complex was only slightly diminished. N1a could not be detected by electron paramagnetic resonance spectroscopy, and unexpectedly, the content of binuclear cluster N1b located on a neighboring subunit was significantly decreased. Because of the lack of N1a and the partial loss of N1b, the variants did not survive detergent extraction from the mutant membranes. Only the C97A(E) variant retained N1a and was purified by chromatographic steps. The prepa...Continue Reading

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Citations

Mar 9, 2021·Biochimica Et Biophysica Acta. Bioenergetics·Kilian ZuchanWolfgang Nitschke
Mar 22, 2018·Chemical Reviews·Wolfgang Buckel, Rudolf K Thauer
Aug 29, 2021·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Ke ZuoPaolo Carloni
Aug 11, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Sabrina OppermannThorsten Friedrich

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